AGRG2_RAT
ID AGRG2_RAT Reviewed; 1013 AA.
AC Q8CJ11; Q8CJ06; Q8CJ07;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Adhesion G-protein coupled receptor G2;
DE AltName: Full=G-protein coupled receptor 64;
DE AltName: Full=Rat epididymis-specific protein 6;
DE Short=Re6;
DE Flags: Precursor;
GN Name=Adgrg2 {ECO:0000312|RGD:628618}; Synonyms=Gpr64, Re6;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), GLYCOSYLATION,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=Lewis; TISSUE=Epididymis;
RX PubMed=12420295; DOI=10.1002/mrd.10220;
RA Obermann H., Samalecos A., Osterhoff C., Schroeder B., Heller R.,
RA Kirchhoff C.;
RT "HE6, a two-subunit heptahelical receptor associated with apical membranes
RT of efferent and epididymal duct epithelia.";
RL Mol. Reprod. Dev. 64:13-26(2003).
CC -!- FUNCTION: Orphan receptor. Could be involved in a signal transduction
CC pathway controlling epididymal function and male fertility. May
CC regulate fluid exchange within epididymis.
CC {ECO:0000250|UniProtKB:Q8CJ12}.
CC -!- SUBUNIT: Heterodimer of 2 chains generated by proteolytic processing;
CC the large extracellular N-terminal fragment and the membrane-bound C-
CC terminal fragment predominantly remain associated and non-covalently
CC linked. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000269|PubMed:12420295}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Long;
CC IsoId=Q8CJ11-1; Sequence=Displayed;
CC Name=2; Synonyms=d2;
CC IsoId=Q8CJ11-2; Sequence=VSP_009810;
CC Name=3; Synonyms=d1;
CC IsoId=Q8CJ11-3; Sequence=VSP_009811;
CC -!- TISSUE SPECIFICITY: Epididymis-specific expression (at protein level).
CC Associated with apical membranes of efferent ductule and proximal
CC epididymal duct epithelia (PubMed:12420295).
CC {ECO:0000269|PubMed:12420295}.
CC -!- PTM: Proteolytically cleaved into 2 subunits, an extracellular subunit
CC and a seven-transmembrane subunit. {ECO:0000305}.
CC -!- PTM: Highly glycosylated. {ECO:0000269|PubMed:12420295}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC Adhesion G-protein coupled receptor (ADGR) subfamily. {ECO:0000305}.
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DR EMBL; AF538953; AAN33055.1; -; mRNA.
DR EMBL; AF538958; AAN33060.1; -; mRNA.
DR EMBL; AF538959; AAN33061.1; -; mRNA.
DR RefSeq; NP_001257800.1; NM_001270871.1. [Q8CJ11-3]
DR RefSeq; NP_001257801.1; NM_001270872.1. [Q8CJ11-2]
DR RefSeq; NP_852031.1; NM_181366.2. [Q8CJ11-1]
DR RefSeq; XP_017457416.1; XM_017601927.1. [Q8CJ11-1]
DR AlphaFoldDB; Q8CJ11; -.
DR SMR; Q8CJ11; -.
DR STRING; 10116.ENSRNOP00000039239; -.
DR MEROPS; P02.007; -.
DR GlyGen; Q8CJ11; 20 sites.
DR PhosphoSitePlus; Q8CJ11; -.
DR PaxDb; Q8CJ11; -.
DR PRIDE; Q8CJ11; -.
DR Ensembl; ENSRNOT00000040770; ENSRNOP00000039239; ENSRNOG00000032472. [Q8CJ11-1]
DR GeneID; 266735; -.
DR KEGG; rno:266735; -.
DR CTD; 10149; -.
DR RGD; 628618; Adgrg2.
DR eggNOG; KOG4193; Eukaryota.
DR GeneTree; ENSGT00940000156341; -.
DR HOGENOM; CLU_002753_3_3_1; -.
DR InParanoid; Q8CJ11; -.
DR OMA; NKTMNVC; -.
DR OrthoDB; 148879at2759; -.
DR PhylomeDB; Q8CJ11; -.
DR TreeFam; TF321769; -.
DR PRO; PR:Q8CJ11; -.
DR Proteomes; UP000002494; Chromosome X.
DR Bgee; ENSRNOG00000032472; Expressed in stomach and 11 other tissues.
DR Genevisible; Q8CJ11; RN.
DR GO; GO:0016324; C:apical plasma membrane; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR Gene3D; 2.60.220.50; -; 1.
DR InterPro; IPR046338; GAIN_dom_sf.
DR InterPro; IPR017981; GPCR_2-like.
DR InterPro; IPR000832; GPCR_2_secretin-like.
DR InterPro; IPR017983; GPCR_2_secretin-like_CS.
DR InterPro; IPR000203; GPS.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF01825; GPS; 1.
DR PRINTS; PR00249; GPCRSECRETIN.
DR SMART; SM00303; GPS; 1.
DR PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; 1.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR PROSITE; PS50221; GPS; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; G-protein coupled receptor;
KW Glycoprotein; Membrane; Phosphoprotein; Receptor; Reference proteome;
KW Signal; Transducer; Transmembrane; Transmembrane helix.
FT SIGNAL 1..37
FT /evidence="ECO:0000255"
FT CHAIN 38..1013
FT /note="Adhesion G-protein coupled receptor G2"
FT /id="PRO_0000012888"
FT TOPO_DOM 38..623
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 624..644
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 645..663
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 664..684
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 685..688
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 689..709
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 710..733
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 734..754
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 755..785
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 786..806
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 807..830
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 831..851
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 852..853
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 854..874
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 875..1013
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 563..614
FT /note="GPS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT MOD_RES 1006
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZP9"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 137
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 155
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 366
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 431
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 452
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 457
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 524
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 538
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 543
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 547
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 593
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 777
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 853
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 40..67
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12420295"
FT /id="VSP_009810"
FT VAR_SEQ 52..67
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12420295"
FT /id="VSP_009811"
SQ SEQUENCE 1013 AA; 110701 MW; 03C5467D84527216 CRC64;
MLFSGGQYSP VGRPEEVLLI YKIFLVIICF HAILVTSLKE NAGNSSLLSP SAESSLVSLV
PYSNGTPDAA SEVLSTLNRT EKSKITILKT FNASGVKSQR NICNLSSICS DSVFFRGEIV
FQHDDHYNVT QNQDIVNSTF AGVLSLSELK RTELNKTLQT LSETYFIVCA TAEAQNTLNC
TFTVKLNETM NVCAMMVTFK SVQIRPMEQC CCSPRTPCPS SPEELEKLQC DLQDPIVCLA
DQPHGPPVSS SSKPVPVVPQ ATIFSHVASD FSLAEPLDHA LMTSSTPSLA QETRLPSPQP
TISLTSSPAI DLPVQHVVAS SSLPQTDLSH TLSPVQSSIP SPTTAAPSVP EKVVAISTPP
GETVVNTSSV PDLEAQVSQM EKALSLGSLE PNLAGEMVNR VSKLLHSPLA LLAPLAQRLL
KVVDAIGLQL NFSSTTISLT SPSLALAVIR VNASNFNTTT FAAQDPANLQ VSLEAQAPKN
SIGAITLPSS LMSNLPASEV ELASRVQFNF FETPALFQDP SLENLSLISY VISSSVTNMT
IKNLTRNVTV ALKHINPSQD DLTVKCVFWD LNRNGGRGGW SSDGCSVKEK RMNETICTCS
HLTSFGILLD LSRTSLPPSQ MMALTFITYI GCGLSSIFLS VTLVTYIAFE KIRRDYPSKI
LIQLCAALLL LNLVFLLDSW IALYNARGFC ISVAVFLHYF LLVSFTWMGL EAFHMYLALV
KVFNTYIRKY ILKFCIVGWG IPAVVVSIVL TISPDNYGIG SYGKFPNGTP DDFCWINSSV
VFYITVVGYF CVIFLLNVSM FIVVLVQLCR IKKKKQLGAQ RKTSIQDLRS IAGLTFLLGI
TWGFAFFAWG PVNLTFMYLF AIFNTLQGFF IFIFYCAAKE NVRKQWRRYL CCGKLRLAEN
SDWSKTATNG LKKQTVNQGV SSSSNSLQSS CNSTNSTTLL VNSDCSVHAS GNGNASTERN
GVSFSVQNGD VCLHDLTGKQ HMFSDKEDSC NGKSRMALRR TSKRGSLHFI EQM
